1ESN
STRUCTURAL BASIS FOR THE FEEDBACK REGULATION OF ESCHERICHIA COLI PANTOTHENATE KINASE BY COENZYME A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004594 | molecular_function | pantothenate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0015937 | biological_process | coenzyme A biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0050165 | molecular_function | pantetheine kinase activity |
| B | 0004594 | molecular_function | pantothenate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0015937 | biological_process | coenzyme A biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0050165 | molecular_function | pantetheine kinase activity |
| C | 0004594 | molecular_function | pantothenate kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0015937 | biological_process | coenzyme A biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016310 | biological_process | phosphorylation |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0050165 | molecular_function | pantetheine kinase activity |
| D | 0004594 | molecular_function | pantothenate kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0015937 | biological_process | coenzyme A biosynthetic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016310 | biological_process | phosphorylation |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0050165 | molecular_function | pantetheine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | SER102 |
| A | GLU199 |
| A | ANP401 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 502 |
| Chain | Residue |
| B | SER102 |
| B | GLU199 |
| B | ANP402 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 503 |
| Chain | Residue |
| C | SER102 |
| C | GLU199 |
| C | ANP403 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 504 |
| Chain | Residue |
| D | SER102 |
| D | GLU199 |
| D | ANP404 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ANP A 401 |
| Chain | Residue |
| A | ASN43 |
| A | ASP45 |
| A | LEU46 |
| A | TYR55 |
| A | VAL97 |
| A | ALA98 |
| A | VAL99 |
| A | GLY100 |
| A | LYS101 |
| A | SER102 |
| A | THR103 |
| A | GLU199 |
| A | ARG243 |
| A | LYS303 |
| A | HIS307 |
| A | MG501 |
| A | HOH5136 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ANP B 402 |
| Chain | Residue |
| B | ASN43 |
| B | ASP45 |
| B | TYR55 |
| B | VAL97 |
| B | ALA98 |
| B | VAL99 |
| B | GLY100 |
| B | LYS101 |
| B | SER102 |
| B | THR103 |
| B | GLU199 |
| B | ARG243 |
| B | LYS303 |
| B | HIS307 |
| B | MG502 |
| B | HOH5077 |
| B | HOH5104 |
| B | HOH5209 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ANP C 403 |
| Chain | Residue |
| C | ASN43 |
| C | ASP45 |
| C | VAL97 |
| C | ALA98 |
| C | VAL99 |
| C | GLY100 |
| C | LYS101 |
| C | SER102 |
| C | THR103 |
| C | GLU199 |
| C | ARG243 |
| C | LYS303 |
| C | HIS307 |
| C | MG503 |
| C | HOH5064 |
| C | HOH5221 |
| C | HOH5263 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ANP D 404 |
| Chain | Residue |
| D | ASN43 |
| D | ASP45 |
| D | TYR55 |
| D | VAL97 |
| D | ALA98 |
| D | VAL99 |
| D | GLY100 |
| D | LYS101 |
| D | SER102 |
| D | THR103 |
| D | ARG243 |
| D | LYS303 |
| D | HIS307 |
| D | MG504 |
| D | HOH5110 |
| D | HOH5306 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY95 | |
| B | GLY95 | |
| C | GLY95 | |
| D | GLY95 |
